The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.
Identifieur interne : 000875 ( PubMed/Corpus ); précédent : 000874; suivant : 000876The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.
Auteurs : J Des Parkin ; James D. San Antonio ; Anton V. Persikov ; Hayat Dagher ; Raymond Dalgleish ; Shane T. Jensen ; Xavier Jeunemaitre ; Judy SavigeSource :
- PloS one [ 1932-6203 ] ; 2017.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites, Collagen Type III (chemistry), Collagen Type III (genetics), Collagen Type III (metabolism), Hemostasis, Humans, Integrin alpha2beta1 (metabolism), Platelet Membrane Glycoproteins (metabolism), Protein Binding, Protein Interaction Maps, Protein Stability, von Willebrand Factor (metabolism).
- MESH :
- chemical , chemistry : Collagen Type III.
- chemical , genetics : Collagen Type III.
- chemical , metabolism : Collagen Type III, Integrin alpha2beta1, Platelet Membrane Glycoproteins, von Willebrand Factor.
- Amino Acid Sequence, Binding Sites, Hemostasis, Humans, Protein Binding, Protein Interaction Maps, Protein Stability.
Abstract
Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.
DOI: 10.1371/journal.pone.0175582
PubMed: 28704418
Links to Exploration step
pubmed:28704418Le document en format XML
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Persikov</name><affiliation><nlm:affiliation>Lewis-Sigler Institute for Integrative Genomics, Princeton University, Carl Icahn Lab, Princeton, NJ, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Dagher, Hayat" sort="Dagher, Hayat" uniqKey="Dagher H" first="Hayat" last="Dagher">Hayat Dagher</name><affiliation><nlm:affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Dalgleish, Raymond" sort="Dalgleish, Raymond" uniqKey="Dalgleish R" first="Raymond" last="Dalgleish">Raymond Dalgleish</name><affiliation><nlm:affiliation>Department of Genetics, University of Leicester, Leicester, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Jensen, Shane T" sort="Jensen, Shane T" uniqKey="Jensen S" first="Shane T" last="Jensen">Shane T. Jensen</name><affiliation><nlm:affiliation>Wharton Business School, University of Pennsylvania, Philadelphia, PA, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Jeunemaitre, Xavier" sort="Jeunemaitre, Xavier" uniqKey="Jeunemaitre X" first="Xavier" last="Jeunemaitre">Xavier Jeunemaitre</name><affiliation><nlm:affiliation>INSERM U970 Paris Cardiovascular Research Centre, Paris France.</nlm:affiliation></affiliation></author><author><name sortKey="Savige, Judy" sort="Savige, Judy" uniqKey="Savige J" first="Judy" last="Savige">Judy Savige</name><affiliation><nlm:affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28704418</idno><idno type="pmid">28704418</idno><idno type="doi">10.1371/journal.pone.0175582</idno><idno type="wicri:Area/PubMed/Corpus">000875</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000875</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.</title><author><name sortKey="Parkin, J Des" sort="Parkin, J Des" uniqKey="Parkin J" first="J Des" last="Parkin">J Des Parkin</name><affiliation><nlm:affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="San Antonio, James D" sort="San Antonio, James D" uniqKey="San Antonio J" first="James D" last="San Antonio">James D. San Antonio</name><affiliation><nlm:affiliation>Operations, Stryker Global Quality and Operations, Malvern, PA, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Persikov, Anton V" sort="Persikov, Anton V" uniqKey="Persikov A" first="Anton V" last="Persikov">Anton V. Persikov</name><affiliation><nlm:affiliation>Lewis-Sigler Institute for Integrative Genomics, Princeton University, Carl Icahn Lab, Princeton, NJ, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Dagher, Hayat" sort="Dagher, Hayat" uniqKey="Dagher H" first="Hayat" last="Dagher">Hayat Dagher</name><affiliation><nlm:affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Dalgleish, Raymond" sort="Dalgleish, Raymond" uniqKey="Dalgleish R" first="Raymond" last="Dalgleish">Raymond Dalgleish</name><affiliation><nlm:affiliation>Department of Genetics, University of Leicester, Leicester, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Jensen, Shane T" sort="Jensen, Shane T" uniqKey="Jensen S" first="Shane T" last="Jensen">Shane T. Jensen</name><affiliation><nlm:affiliation>Wharton Business School, University of Pennsylvania, Philadelphia, PA, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Jeunemaitre, Xavier" sort="Jeunemaitre, Xavier" uniqKey="Jeunemaitre X" first="Xavier" last="Jeunemaitre">Xavier Jeunemaitre</name><affiliation><nlm:affiliation>INSERM U970 Paris Cardiovascular Research Centre, Paris France.</nlm:affiliation></affiliation></author><author><name sortKey="Savige, Judy" sort="Savige, Judy" uniqKey="Savige J" first="Judy" last="Savige">Judy Savige</name><affiliation><nlm:affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Collagen Type III (chemistry)</term><term>Collagen Type III (genetics)</term><term>Collagen Type III (metabolism)</term><term>Hemostasis</term><term>Humans</term><term>Integrin alpha2beta1 (metabolism)</term><term>Platelet Membrane Glycoproteins (metabolism)</term><term>Protein Binding</term><term>Protein Interaction Maps</term><term>Protein Stability</term><term>von Willebrand Factor (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Collagen Type III</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Collagen Type III</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Collagen Type III</term><term>Integrin alpha2beta1</term><term>Platelet Membrane Glycoproteins</term><term>von Willebrand Factor</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Hemostasis</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Maps</term><term>Protein Stability</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28704418</PMID><DateCreated><Year>2017</Year><Month>07</Month><Day>13</Day></DateCreated><DateCompleted><Year>2017</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>20</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>7</Issue><PubDate><Year>2017</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.</ArticleTitle><Pagination><MedlinePgn>e0175582</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0175582</ELocationID><Abstract><AbstractText>Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Parkin</LastName><ForeName>J Des</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>San Antonio</LastName><ForeName>James D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Operations, Stryker Global Quality and Operations, Malvern, PA, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Persikov</LastName><ForeName>Anton V</ForeName><Initials>AV</Initials><AffiliationInfo><Affiliation>Lewis-Sigler Institute for Integrative Genomics, Princeton University, Carl Icahn Lab, Princeton, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dagher</LastName><ForeName>Hayat</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dalgleish</LastName><ForeName>Raymond</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Genetics, University of Leicester, Leicester, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jensen</LastName><ForeName>Shane T</ForeName><Initials>ST</Initials><AffiliationInfo><Affiliation>Wharton Business School, University of Pennsylvania, Philadelphia, PA, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jeunemaitre</LastName><ForeName>Xavier</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>INSERM U970 Paris Cardiovascular Research Centre, Paris France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University Paris Descartes, Paris Sorbonne Cite, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Savige</LastName><ForeName>Judy</ForeName><Initials>J</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-6813-0288</Identifier><AffiliationInfo><Affiliation>From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>07</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024061">Collagen Type III</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D038982">Integrin alpha2beta1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010980">Platelet Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C098341">platelet membrane glycoprotein VI</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014841">von Willebrand Factor</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7275-80</RefSource><PMID 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alpha2beta1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010980" MajorTopicYN="N">Platelet Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060066" MajorTopicYN="N">Protein Interaction Maps</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014841" MajorTopicYN="N">von Willebrand Factor</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>01</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>03</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>7</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>7</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>9</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28704418</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0175582</ArticleId><ArticleId IdType="pii">PONE-D-17-00972</ArticleId><ArticleId IdType="pmc">PMC5509119</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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